cyclase family protein is a metal dependent hydrolase which may contain a conserved motif HXGTHXDXPXH that is likely to form part of the active site; similar to kynurenine formamidase that catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in ...
3-208
1.23e-122
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in proteins involved in antibiotic synthesis. However they are also found in organizms that do not make antibiotics pointing to a wider role for these proteins. The proteins contain a conserved motif HXGTHXDXPXH that is likely to form part of the active site.
The actual alignment was detected with superfamily member TIGR03035:
Pssm-ID: 469937 Cd Length: 206 Bit Score: 345.56 E-value: 1.23e-122
arylformamidase; One of several pathways of tryptophan degradation is as follows: tryptophan 2, ...
3-208
1.23e-122
arylformamidase; One of several pathways of tryptophan degradation is as follows: tryptophan 2,3-dioxygenase (1.13.11.11) uses 02 to convert Trp to L-formylkynurenine. Arylformamidase (3.5.1.9) hydrolyzes the product to L-kynurenine and formate. Kynureninase (3.7.1.3) hydrolyzes L-kynurenine to anthranilate plus alanine. Members of the seed alignment for this model are bacterial predicted metal-dependent hydrolases. All are supported as arylformamidase (3.5.1.9) by an operon structure in which kynureninase and/or tryptophan 2,3-dioxygenase genes are adjacent. The members from Bacillus cereus, Pseudomonas aeruginosa and Ralstonia metallidurans were characterized. An example from Pseudomonas fluorescens is given the gene symbol qbsH instead of kynB because of its role in quinolobactin biosynthesis, which begins with tryptophan. All members of this family should be arylformamidase (3.5.1.9). [Energy metabolism, Amino acids and amines]
Pssm-ID: 132080 Cd Length: 206 Bit Score: 345.56 E-value: 1.23e-122
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in ...
6-151
1.26e-30
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in proteins involved in antibiotic synthesis. However they are also found in organizms that do not make antibiotics pointing to a wider role for these proteins. The proteins contain a conserved motif HXGTHXDXPXH that is likely to form part of the active site.
Pssm-ID: 461224 Cd Length: 159 Bit Score: 110.03 E-value: 1.26e-30
Mth938 domain. Mth938 is a hypothetical protein encoded by the Methanobacterium ...
84-147
5.69e-03
Mth938 domain. Mth938 is a hypothetical protein encoded by the Methanobacterium thermoautotrophicum (Mth) genome. This protein crystallizes as a dimer, although it is monomeric in solution, with one disulfide bond in each monomer. The function of the protein has not been determined.
Pssm-ID: 240162 Cd Length: 117 Bit Score: 35.39 E-value: 5.69e-03
arylformamidase; One of several pathways of tryptophan degradation is as follows: tryptophan 2, ...
3-208
1.23e-122
arylformamidase; One of several pathways of tryptophan degradation is as follows: tryptophan 2,3-dioxygenase (1.13.11.11) uses 02 to convert Trp to L-formylkynurenine. Arylformamidase (3.5.1.9) hydrolyzes the product to L-kynurenine and formate. Kynureninase (3.7.1.3) hydrolyzes L-kynurenine to anthranilate plus alanine. Members of the seed alignment for this model are bacterial predicted metal-dependent hydrolases. All are supported as arylformamidase (3.5.1.9) by an operon structure in which kynureninase and/or tryptophan 2,3-dioxygenase genes are adjacent. The members from Bacillus cereus, Pseudomonas aeruginosa and Ralstonia metallidurans were characterized. An example from Pseudomonas fluorescens is given the gene symbol qbsH instead of kynB because of its role in quinolobactin biosynthesis, which begins with tryptophan. All members of this family should be arylformamidase (3.5.1.9). [Energy metabolism, Amino acids and amines]
Pssm-ID: 132080 Cd Length: 206 Bit Score: 345.56 E-value: 1.23e-122
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in ...
6-151
1.26e-30
Putative cyclase; Proteins in this family are thought to be cyclase enzymes. They are found in proteins involved in antibiotic synthesis. However they are also found in organizms that do not make antibiotics pointing to a wider role for these proteins. The proteins contain a conserved motif HXGTHXDXPXH that is likely to form part of the active site.
Pssm-ID: 461224 Cd Length: 159 Bit Score: 110.03 E-value: 1.26e-30
Mth938 domain. Mth938 is a hypothetical protein encoded by the Methanobacterium ...
84-147
5.69e-03
Mth938 domain. Mth938 is a hypothetical protein encoded by the Methanobacterium thermoautotrophicum (Mth) genome. This protein crystallizes as a dimer, although it is monomeric in solution, with one disulfide bond in each monomer. The function of the protein has not been determined.
Pssm-ID: 240162 Cd Length: 117 Bit Score: 35.39 E-value: 5.69e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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